Osmolyte-induced folding enhances tryptic enzyme activity
Osmolyte-induced folding enhances tryptic enzyme activity
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DOI：
10.1016/j.abb.2005.01.008
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发表时间：
2005-04-01
影响因子：
3.9
通讯作者：
Thompson, EB
中科院分区：
文献类型：
--
作者：
Kumar, R;Serrette, JM;Thompson, EB
渗透剂形成一类天然存在的小化合物，已知其保护蛋白质处于其天然折叠和功能状态。在渗透剂中，三甲胺-N-氧化物（TMAO）最近受到特别的关注，因为它显示出非凡的能力来支持变性的天然样物质的折叠，其显示出显著的功能活性。大多数酶和/或蛋白质通常储存在甘油中以保持其活性/功能。在本研究中，我们测试了TMAO是否可以是一个更好的溶质比甘油两种常用的蛋白酶，胰蛋白酶和胰凝乳蛋白酶。我们的酶动力学数据表明，胰蛋白酶的酶活性显着增强TMAO相比，甘油，而胰凝乳蛋白酶的活性没有显着改变，在任何情况下。这些结果是根据这些酶的折叠的渗透剂的影响，从荧光发射光谱的数据判断。这些结果表明，TMAO可能是比甘油更好的溶质，以保持最佳的胰蛋白酶活性。(c)2005年爱思唯尔公司All rights reserved.
Osmolytes form a class of naturally occurring small compounds known to protect proteins in their native folded and functional states. Among the osmolytes, trimethylamine-N-oxide (TMAO) has received special interest lately because it has shown an extraordinary capability to support folding of denatured to native-like species, which show significant functional activity. Most enzymes and/or proteins are commonly stored in glycerol to maintain their activity/function. In the present study, we tested whether TMAO can be a better solute than glycerol for two commonly used proteases, trypsin and chymotrypsin. Our enzyme kinetic data suggest that the enzyme activity of trypsin is significantly enhanced in TMAO compared to glycerol, whereas chymotrypsin activity is not significantly changed in either case. These results are in accordance with the osmolyte effects on the folding of these enzymes, as judged by data from fluorescence emission spectroscopy. These results Suggest that TMAO may be a better solute than glycerol to maintain optimal tryptic enzyme activity. (c) 2005 Elsevier Inc. All rights reserved.